|
Name |
Accession |
Description |
Interval |
E-value |
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
22-399 |
1.02e-125 |
|
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and metabolism]; Acyl-CoA dehydrogenase related to the alkylation response protein AidB is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 441563 [Multi-domain] Cd Length: 381 Bit Score: 367.63 E-value: 1.02e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 22 FDDAHRTLAEGLVPWAA------AQEVDEtdDRAACRDWVQRLGAGGWLRYCVPAAHGGAlpALDSRALVLLRETLAYHS 95
Cdd:COG1960 5 LTEEQRALRDEVREFAEeeiapeAREWDR--EGEFPRELWRKLAELGLLGLTIPEEYGGL--GLSLVELALVLEELARAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 96 PLADFAFAMQGLGSGAITLAGSPAQQAHYLQGVARGELIAAFALSEPEAGSDVSAMQTVATSaypstasgKEHSYSLTGT 175
Cdd:COG1960 81 ASLALPVGVHNGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVR--------DGDGYVLNGQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 176 KTWISNGGIADFYCVFAKTDPAGGTRGISAFIVDANTPGLDASRHIHVMAPH--PLATLLFTNCTVPATALLGEENGGFK 253
Cdd:COG1960 153 KTFITNAPVADVILVLARTDPAAGHRGISLFLVPKDTPGVTVGRIEDKMGLRgsDTGELFFDDVRVPAENLLGEEGKGFK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 254 LAMRTLDIFRASVAAAALGMARRALAEAVHHARQRRMFGQTLADFQLTQARIGEMAALVDSAALLTYRAAWLRDQGQArV 333
Cdd:COG1960 233 IAMSTLNAGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGED-A 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496182615 334 TAEAAMAKMTATENAQRVIDMALQLHGGRGVEVGSKVESLYRDIRSLRIYEGATEVQQLIIGKAAL 399
Cdd:COG1960 312 ALEAAMAKLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLL 377
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
99-396 |
9.75e-102 |
|
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal acyl-CoA oxidases (AXO) catalyze the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. In contrast, AXO catalyzes a different oxidative half-reaction, in which the reduced FAD is reoxidized by molecular oxygen. The ACAD family includes the eukaryotic beta-oxidation enzymes, short (SCAD), medium (MCAD), long (LCAD) and very-long (VLCAD) chain acyl-CoA dehydrogenases. These enzymes all share high sequence similarity, but differ in their substrate specificities. The ACAD family also includes amino acid catabolism enzymes such as Isovaleryl-CoA dehydrogenase (IVD), short/branched chain acyl-CoA dehydrogenases(SBCAD), Isobutyryl-CoA dehydrogenase (IBDH), glutaryl-CoA deydrogenase (GCD) and Crotonobetainyl-CoA dehydrogenase. The mitochondrial ACAD's are generally homotetramers, except for VLCAD, which is a homodimer. Related enzymes include the SOS adaptive reponse proten aidB, Naphthocyclinone hydroxylase (NcnH), and and Dibenzothiophene (DBT) desulfurization enzyme C (DszC)
Pssm-ID: 173838 [Multi-domain] Cd Length: 327 Bit Score: 304.59 E-value: 9.75e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 99 DFAFAMQGLGSGAITLAGSPAQQAHYLQGVARGELIAAFALSEPEAGSDVSAMQTVATsaypstASGKEhsYSLTGTKTW 178
Cdd:cd00567 35 LLAELGLLLGAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTAR------KDGDG--YVLNGRKIF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 179 ISNGGIADFYCVFAKTDPAG-GTRGISAFIVDANTPGLDASRHIHV--MAPHPLATLLFTNCTVPATALLGEENGGFKLA 255
Cdd:cd00567 107 ISNGGDADLFIVLARTDEEGpGHRGISAFLVPADTPGVTVGRIWDKmgMRGSGTGELVFDDVRVPEDNLLGEEGGGFELA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 256 MRTLDIFRASVAAAALGMARRALAEAVHHARQRRMFGQTLADFQLTQARIGEMAALVDSAALLTYRAAWLRDQGQARVTA 335
Cdd:cd00567 187 MKGLNVGRLLLAAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDEARL 266
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496182615 336 EAAMAKMTATENAQRVIDMALQLHGGRGVEVGSKVESLYRDIRSLRIYEGATEVQQLIIGK 396
Cdd:cd00567 267 EAAMAKLFATEAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
33-399 |
4.71e-100 |
|
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA dehydrogenases; Short chain acyl-CoA dehydrogenase (SCAD). SCAD is a mitochondrial beta-oxidation enzyme. It catalyzes the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of SCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. This subgroup also contains the eukaryotic short/branched chain acyl-CoA dehydrogenase(SBCAD), the bacterial butyryl-CoA dehydorgenase(BCAD) and 2-methylbutyryl-CoA dehydrogenase, which is involved in isoleucine catabolism. These enzymes are homotetramers.
Pssm-ID: 173847 [Multi-domain] Cd Length: 373 Bit Score: 301.88 E-value: 4.71e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 33 LVPWAAaqEVDETDdrAACRDWVQRLGAGGWLRYCVPAAHGGAlpALDSRALVLLRETLAYHSPLADFAFAMQ-GLGSGA 111
Cdd:cd01158 18 IAPLAA--EMDEKG--EFPREVIKEMAELGLMGIPIPEEYGGA--GLDFLAYAIAIEELAKVDASVAVIVSVHnSLGANP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 112 ITLAGSPAQQAHYLQGVARGELIAAFALSEPEAGSDVSAMQTvatsaypsTASGKEHSYSLTGTKTWISNGGIADFYCVF 191
Cdd:cd01158 92 IIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKT--------TAKKDGDDYVLNGSKMWITNGGEADFYIVF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 192 AKTDPAGGTRGISAFIVDANTPGLDASRHIHVMAPH--PLATLLFTNCTVPATALLGEENGGFKLAMRTLDIFRASVAAA 269
Cdd:cd01158 164 AVTDPSKGYRGITAFIVERDTPGLSVGKKEDKLGIRgsSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGGRIGIAAQ 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 270 ALGMARRALAEAVHHARQRRMFGQTLADFQLTQARIGEMAALVDSAALLTYRAAWLRDQGQArVTAEAAMAKMTATENAQ 349
Cdd:cd01158 244 ALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEP-FIKEAAMAKLFASEVAM 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 496182615 350 RVIDMALQLHGGRGVEVGSKVESLYRDIRSLRIYEGATEVQQLIIGKAAL 399
Cdd:cd01158 323 RVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHLL 372
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
52-400 |
5.61e-75 |
|
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is found in the mitochondria of eukaryotes and in some bacteria. It catalyzes the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. VLCAD acts as a homodimer.
Pssm-ID: 173850 [Multi-domain] Cd Length: 409 Bit Score: 238.91 E-value: 5.61e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 52 RDWVQRLGAGGWLRYCVPAAHGGAlpALDSRALVLLRETLAYHSPLADFAFAMQGLGSGAITLAGSPAQQAHYLQGVARG 131
Cdd:cd01161 59 RKTLTQLKELGLFGLQVPEEYGGL--GLNNTQYARLAEIVGMDLGFSVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASG 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 132 ELIAAFALSEPEAGSDVSAMQTVATSaypsTASGKehSYSLTGTKTWISNGGIADFYCVFAKT---DPAGGTR-GISAFI 207
Cdd:cd01161 137 EWIAAFALTEPSSGSDAASIRTTAVL----SEDGK--HYVLNGSKIWITNGGIADIFTVFAKTevkDATGSVKdKITAFI 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 208 VD------ANTP-----GLDASRhihvmaphpLATLLFTNCTVPATALLGEENGGFKLAMRTLDIFRASVAAAALGMARR 276
Cdd:cd01161 211 VErsfggvTNGPpekkmGIKGSN---------TAEVYFEDVKIPVENVLGEVGDGFKVAMNILNNGRFGMGAALIGTMKR 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 277 ALAEAVHHARQRRMFGQTLADFQLTQARIGEMAALVDSAALLTYRAAWLRDQG-QARVTAEAAMAKMTATENAQRVIDMA 355
Cdd:cd01161 282 CIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESMAYMTSGNMDRGlKAEYQIEAAISKVFASEAAWLVVDEA 361
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 496182615 356 LQLHGGRGVEVGSKVESLYRDIRSLRIYEGATEVQQLIIGKAALQ 400
Cdd:cd01161 362 IQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFIALTGLQ 406
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
21-396 |
1.28e-73 |
|
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found in the mitochondria of eukaryotes and in some prokaryotes. It catalyzes the alpha, beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of LCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. LCAD acts as a homodimer.
Pssm-ID: 173849 [Multi-domain] Cd Length: 372 Bit Score: 234.32 E-value: 1.28e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 21 FFDDAHRTLAEGLVPWAAAQEVDETDDRAACRdwvqRLGAGGWLRYCVPAAHGGAlpALDSRALVLLRETLAYHSPLADF 100
Cdd:cd01160 6 FRDVVRRFFAKEVAPFHHEWEKAGEVPREVWR----KAGEQGLLGVGFPEEYGGI--GGDLLSAAVLWEELARAGGSGPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 101 AFAMQGLGSGAITLAGSPAQQAHYLQGVARGELIAAFALSEPEAGSDVSAMQTvatsaypsTASGKEHSYSLTGTKTWIS 180
Cdd:cd01160 80 LSLHTDIVSPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRT--------TARKDGDHYVLNGSKTFIT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 181 NGGIADFYCVFAKTD-PAGGTRGISAFIVDANTPGLDASRHIHVMA--PHPLATLLFTNCTVPATALLGEENGGFKLAMR 257
Cdd:cd01160 152 NGMLADVVIVVARTGgEARGAGGISLFLVERGTPGFSRGRKLKKMGwkAQDTAELFFDDCRVPAENLLGEENKGFYYLMQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 258 TLDIFRASVAAAALGMARRALAEAVHHARQRRMFGQTLADFQLTQARIGEMAALVDSAALLTYRAAWLRDQGQArVTAEA 337
Cdd:cd01160 232 NLPQERLLIAAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRL-DVAEA 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 496182615 338 AMAKMTATENAQRVIDMALQLHGGRGVEVGSKVESLYRDIRSLRIYEGATEVQQLIIGK 396
Cdd:cd01160 311 SMAKYWATELQNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISR 369
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
22-397 |
6.54e-68 |
|
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA dehydrogenase, which catalyzes the third step in leucine catabolism, the conversion of isovaleryl-CoA (3-methylbutyryl-CoA) into 3-methylcrotonyl-CoA. IVD is a homotetramer and has the greatest affinity for small branched chain substrates.
Pssm-ID: 173845 [Multi-domain] Cd Length: 376 Bit Score: 219.59 E-value: 6.54e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 22 FDDAHRTLAEGLVPWAA------AQEVDETDDRAacRDWVQRLGAGGWLRYCVPAAHGGAlpALDSRALVLLRETLAYHS 95
Cdd:cd01156 2 LDDEIEMLRQSVREFAQkeiaplAAKIDRDNEFP--RDLWRKMGKLGLLGITAPEEYGGS--GMGYLAHVIIMEEISRAS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 96 PLADFAF-AMQGLGSGAITLAGSPAQQAHYLQGVARGELIAAFALSEPEAGSDVSAMQTVATSaypstasgKEHSYSLTG 174
Cdd:cd01156 78 GSVALSYgAHSNLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEK--------KGDRYVLNG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 175 TKTWISNGGIADFYCVFAKTDPAGGTRGISAFIVDANTPGLDASRHIHV--MAPHPLATLLFTNCTVPATALLGEENGGF 252
Cdd:cd01156 150 SKMWITNGPDADTLVVYAKTDPSAGAHGITAFIVEKGMPGFSRAQKLDKlgMRGSNTCELVFEDCEVPEENILGGENKGV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 253 KLAMRTLDIFRASVAAAALGMARRALAEAVHHARQRRMFGQTLADFQLTQARIGEMAALVDSAALLTYRAAWLRDQGQaR 332
Cdd:cd01156 230 YVLMSGLDYERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGN-M 308
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496182615 333 VTAEAAMAKMTATENAQRVIDMALQLHGGRGVEVGSKVESLYRDIRSLRIYEGATEVQQLIIGKA 397
Cdd:cd01156 309 DPKDAAGVILYAAEKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVIGRE 373
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
58-401 |
8.93e-64 |
|
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- dehydrogenation of short branched chain acyl-CoA intermediates in valine catabolism. It is predicted to be a homotetramer.
Pssm-ID: 173851 [Multi-domain] Cd Length: 375 Bit Score: 208.84 E-value: 8.93e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 58 LGAGGWlrYCVPAAHGGALPALDSralVLLRETLAYHSPLADFAFAMQGLGSGAITLAGSPAQQAHYLQGVARGELIAAF 137
Cdd:cd01162 44 LGFGGI--YIRDDVGGSGLSRLDA---SIIFEALSTGCVSTAAYISIHNMCAWMIDSFGNDEQRERFLPDLCTMEKLASY 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 138 ALSEPEAGSDVSAMQTvatsaypsTASGKEHSYSLTGTKTWISNGGIADFYCVFAKTDpAGGTRGISAFIVDANTPGLDA 217
Cdd:cd01162 119 CLTEPGSGSDAAALRT--------RAVREGDHYVLNGSKAFISGAGDSDVYVVMARTG-GEGPKGISCFVVEKGTPGLSF 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 218 SRHIHVMAPH--PLATLLFTNCTVPATALLGEENGGFKLAMRTLDIFRASVAAAALGMARRALAEAVHHARQRRMFGQTL 295
Cdd:cd01162 190 GANEKKMGWNaqPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLNGGRLNIASCSLGAAQAALDLARAYLEERKQFGKPL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 296 ADFQLTQARIGEMAALVDSAALLTYRAAWLRDQGQARVTAEAAMAKMTATENAQRVIDMALQLHGGRGVEVGSKVESLYR 375
Cdd:cd01162 270 ADFQALQFKLADMATELVASRLMVRRAASALDRGDPDAVKLCAMAKRFATDECFDVANQALQLHGGYGYLKDYPVEQYVR 349
|
330 340
....*....|....*....|....*.
gi 496182615 376 DIRSLRIYEGATEVQQLIIGKAALQE 401
Cdd:cd01162 350 DLRVHQILEGTNEIMRLIIARALLTR 375
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
22-396 |
4.29e-63 |
|
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which catalyze the alpha,beta dehydrogenation of the corresponding medium chain acyl-CoA by FAD, which becomes reduced. The reduced form of MCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. MCAD is a homotetramer.
Pssm-ID: 173846 [Multi-domain] Cd Length: 378 Bit Score: 207.05 E-value: 4.29e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 22 FDDAHRTLA-EGLVPWAAaqEVDETDDRAAcrDWVQRLGAGGWLRYCVPAAHGGalPALDSRALVLLRETLAYHSPLADF 100
Cdd:cd01157 8 FQETARKFArEEIIPVAA--EYDKSGEYPW--PLIKRAWELGLMNTHIPEDCGG--LGLGTFDTCLITEELAYGCTGVQT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 101 AFAMQGLGSGAITLAGSPAQQAHYLQGVARGELIAAFALSEPEAGSDVSAMQTvatsaypsTASGKEHSYSLTGTKTWIS 180
Cdd:cd01157 82 AIEANSLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKT--------KAEKKGDEYIINGQKMWIT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 181 NGGIADFYCVFAKTDP---AGGTRGISAFIVDANTPGLDASRHIHVMAPHPLAT--LLFTNCTVPATALLGEENGGFKLA 255
Cdd:cd01157 154 NGGKANWYFLLARSDPdpkCPASKAFTGFIVEADTPGIQPGRKELNMGQRCSDTrgITFEDVRVPKENVLIGEGAGFKIA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 256 MRTLDIFRASVAAAALGMARRALAEAVHHARQRRMFGQTLADFQLTQARIGEMAALVDSAALLTYRAAWLRDQGQaRVTA 335
Cdd:cd01157 234 MGAFDKTRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGR-RNTY 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496182615 336 EAAMAKMTATENAQRVIDMALQLHGGRGVEVGSKVESLYRDIRSLRIYEGATEVQQLIIGK 396
Cdd:cd01157 313 YASIAKAFAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISR 373
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
23-397 |
3.17e-58 |
|
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, which catalyzes the oxidative decarboxylation of glutaryl-CoA to crotonyl-CoA and carbon dioxide in the catabolism of lysine, hydroxylysine, and tryptophan. It uses electron transfer flavoprotein (ETF) as an electron acceptor. GCD is a homotetramer. GCD deficiency leads to a severe neurological disorder in humans.
Pssm-ID: 173840 [Multi-domain] Cd Length: 386 Bit Score: 194.50 E-value: 3.17e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 23 DDAHRTLAEGLVPWAAAQEVDETDDRaacrDWVQRLGAGGWLRyCVPAAHGGalPALDSRALVLL-RETLAYHSPLADFA 101
Cdd:cd01151 22 DTAREFCQEELAPRVLEAYREEKFDR----KIIEEMGELGLLG-ATIKGYGC--AGLSSVAYGLIaREVERVDSGYRSFM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 102 FAMQGLGSGAITLAGSPAQQAHYLQGVARGELIAAFALSEPEAGSDVSAMQTvatsaypsTASGKEHSYSLTGTKTWISN 181
Cdd:cd01151 95 SVQSSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMET--------RARKDGGGYKLNGSKTWITN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 182 GGIADFYCVFAKTDPAGGTRGisaFIVDANTPGLDASRHIHVMAPHPLAT--LLFTNCTVPATALLGEENgGFKLAMRTL 259
Cdd:cd01151 167 SPIADVFVVWARNDETGKIRG---FILERGMKGLSAPKIQGKFSLRASITgeIVMDNVFVPEENLLPGAE-GLRGPFKCL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 260 DIFRASVAAAALGMARRALAEAVHHARQRRMFGQTLADFQLTQARIGEMAALVDSAALLTYRAAWLRDQGQARvTAEAAM 339
Cdd:cd01151 243 NNARYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVGRLKDQGKAT-PEQISL 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 496182615 340 AKMTATENAQRVIDMALQLHGGRGVEVGSKVESLYRDIRSLRIYEGATEVQQLIIGKA 397
Cdd:cd01151 322 LKRNNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIHALILGRA 379
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
21-400 |
2.76e-51 |
|
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA dehydrogenases (ACAD). Mitochondrial acyl-CoA dehydrogenases (ACAD) catalyze the alpha, beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. The mitochondrial ACD's are generally homotetramers and have an active site glutamate at a conserved position.
Pssm-ID: 173841 [Multi-domain] Cd Length: 380 Bit Score: 176.38 E-value: 2.76e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 21 FFDDAHRTLAEGLVP-WAAAQEVDETDDRAACRDWVQRLGAGGWLRYCVPAAHGGAlpALDSRALVLLRETLAYHSPLAD 99
Cdd:cd01152 6 FRAEVRAWLAAHLPPeLREESALGYREGREDRRRWQRALAAAGWAAPGWPKEYGGR--GASLMEQLIFREEMAAAGAPVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 100 FAFAMQGLGSGAITLAGSPAQQAHYLQGVARGELIAAFALSEPEAGSDVSAMQTvatsaypsTASGKEHSYSLTGTKTWI 179
Cdd:cd01152 84 FNQIGIDLAGPTILAYGTDEQKRRFLPPILSGEEIWCQGFSEPGAGSDLAGLRT--------RAVRDGDDWVVNGQKIWT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 180 SNGGIADFYCVFAKTDPAGGT-RGISAFIVDANTPGLDASRHIHVMAPHPLATLLFTNCTVPATALLGEENGGFKLAMRT 258
Cdd:cd01152 156 SGAHYADWAWLLVRTDPEAPKhRGISILLVDMDSPGVTVRPIRSINGGEFFNEVFLDDVRVPDANRVGEVNDGWKVAMTT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 259 LDIFRASVAAAALGMARRALAEAVHHARQRRmfgqTLADFQLTQARIGEMAALVDSAALLTYRAAWLRDQGQaRVTAEAA 338
Cdd:cd01152 236 LNFERVSIGGSAATFFELLLARLLLLTRDGR----PLIDDPLVRQRLARLEAEAEALRLLVFRLASALAAGK-PPGAEAS 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 339 MAKMTATENAQRVIDMALQLHGGRGV--------EVGSKVESLYRDIRSLRIYEGATEVQQLIIGKAALQ 400
Cdd:cd01152 311 IAKLFGSELAQELAELALELLGTAALlrdpapgaELAGRWEADYLRSRATTIYGGTSEIQRNIIAERLLG 380
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
52-401 |
1.89e-50 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 174.74 E-value: 1.89e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 52 RDWVQRLGAGGWLRYCVPAAHGGAlpALDSRALVLLRETLAYHSP---LADFAFAMqgLGSGAITLAGSPAQQAHYLQGV 128
Cdd:PTZ00461 71 RDLFKQLGDLGVMGVTVPEADGGA--GMDAVAAVIIHHELSKYDPgfcLAYLAHSM--LFVNNFYYSASPAQRARWLPKV 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 129 ARGELIAAFALSEPEAGSDVSAMQTVATSaypsTASGKehsYSLTGTKTWISNGGIADFYCVFAKTDPAggtrgISAFIV 208
Cdd:PTZ00461 147 LTGEHVGAMGMSEPGAGTDVLGMRTTAKK----DSNGN---YVLNGSKIWITNGTVADVFLIYAKVDGK-----ITAFVV 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 209 DANTPGLDASRHIHV--MAPHPLATLLFTNCTVPATALLGEENGGFKLAMRTLDIFRASVAAAALGMARRALAEAVHHAR 286
Cdd:PTZ00461 215 ERGTKGFTQGPKIDKcgMRASHMCQLFFEDVVVPAENLLGEEGKGMVGMMRNLELERVTLAAMAVGIAERSVELMTSYAS 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 287 QRRMFGQTLADFQLTQARIGEMAALVDSAALLTYRAAW-LRDQGQARVTAEAamAKMTATENAQRVIDMALQLHGGRGVE 365
Cdd:PTZ00461 295 ERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHnVHPGNKNRLGSDA--AKLFATPIAKKVADSAIQVMGGMGYS 372
|
330 340 350
....*....|....*....|....*....|....*.
gi 496182615 366 VGSKVESLYRDIRSLRIYEGATEVQQLIIGKAALQE 401
Cdd:PTZ00461 373 RDMPVERLWRDAKLLEIGGGTIEAHHKNITKDLLKG 408
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
68-401 |
2.42e-50 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 173.76 E-value: 2.42e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 68 VPAAHGGAlPAlDSRALVLLRETLAYHSplADFAFAMQGLGSGAITLAGSPAQQAH-YLQGVARGELIAAFALSEPEAGS 146
Cdd:PRK12341 56 VPEEFGGT-PA-DYVTQMLVLEEVSKCG--APAFLITNGQCIHSMRRFGSAEQLRKtAESTLETGDPAYALALTEPGAGS 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 147 DVSAMQTVATSAypstaSGKEHsysLTGTKTWISNGGIADFYCVFAK-TDPAGGTRGISAFIVDANTPGLDASRhIHVMA 225
Cdd:PRK12341 132 DNNSATTTYTRK-----NGKVY---LNGQKTFITGAKEYPYMLVLARdPQPKDPKKAFTLWWVDSSKPGIKINP-LHKIG 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 226 PHPLAT--LLFTNCTVPATALLGEENGGFKLAMRTLDIFRASVAAAALGMARRALAEAVHHARQRRMFGQTLADFQLTQA 303
Cdd:PRK12341 203 WHMLSTceVYLDNVEVEESDLVGEEGMGFLNVMYNFEMERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQE 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 304 RIGEMAALVDSAALLTYRAAWLRDQGQArVTAEAAMAKMTATENAQRVIDMALQLHGGRGVEVGSKVESLYRDIRSLRIY 383
Cdd:PRK12341 283 KLTLMAIKIENMRNMVYKVAWQADNGQS-LRTSAALAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIG 361
|
330
....*....|....*...
gi 496182615 384 EGATEVQQLIIGKAALQE 401
Cdd:PRK12341 362 GGTDEIMIYIAGRQILKD 379
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
116-401 |
9.06e-47 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 165.05 E-value: 9.06e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 116 GSPAQQAHYLQGVARGELIAAFALSEPEAGSDVSAMQTvatsaypsTASGKEHSYSLTGTKTWISNGGIADFYCVFAKTD 195
Cdd:PLN02519 125 GTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKC--------KAERVDGGYVLNGNKMWCTNGPVAQTLVVYAKTD 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 196 PAGGTRGISAFIVDANTPGLDASRHIHV--MAPHPLATLLFTNCTVPATALLGEENGGFKLAMRTLDIFRASVAAAALGM 273
Cdd:PLN02519 197 VAAGSKGITAFIIEKGMPGFSTAQKLDKlgMRGSDTCELVFENCFVPEENVLGQEGKGVYVMMSGLDLERLVLAAGPLGL 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 274 ARRALAEAVHHARQRRMFGQTLADFQLTQARIGEMAALVDSAALLTYRAAWLRDQGQARvTAEAAMAKMTATENAQRVID 353
Cdd:PLN02519 277 MQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVD-RKDCAGVILCAAERATQVAL 355
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 496182615 354 MALQLHGGRGVEVGSKVESLYRDIRSLRIYEGATEVQQLIIGKAALQE 401
Cdd:PLN02519 356 QAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGRELFKE 403
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
249-398 |
5.17e-45 |
|
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an all-alpha, four helical up-and-down bundle.
Pssm-ID: 395354 [Multi-domain] Cd Length: 149 Bit Score: 152.41 E-value: 5.17e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 249 NGGFKLAMRTLDIFRASVAAAALGMARRALAEAVHHARQRRMFGQTLADFQLTQARIGEMAALVDSAALLTYRAAWLRDQ 328
Cdd:pfam00441 1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 329 GQArVTAEAAMAKMTATENAQRVIDMALQLHGGRGVEVGSKVESLYRDIRSLRIYEGATEVQQLIIGKAA 398
Cdd:pfam00441 81 GGP-DGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIARRL 149
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
116-400 |
1.47e-44 |
|
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA dehydrogenases (ACAD) catalyze the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACAD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. ACAD's are generally homotetramers and have an active site glutamate at a conserved position.
Pssm-ID: 173844 [Multi-domain] Cd Length: 394 Bit Score: 158.71 E-value: 1.47e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 116 GSPAQQAHYLQGVARGELIAAFALSEPE-AGSDVSAMQTvatsaypsTASGKEHSYSLTGTKTWISNGGIAD--FYCVFA 192
Cdd:cd01155 108 GSEEQKKQWLEPLLDGKIRSAFAMTEPDvASSDATNIEC--------SIERDGDDYVINGRKWWSSGAGDPRckIAIVMG 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 193 KTDPAGGTRGI--SAFIVDANTPGLDASRHIHVM----APHPLATLLFTNCTVPATALLGEENGGFKLAMRTLDIFRASV 266
Cdd:cd01155 180 RTDPDGAPRHRqqSMILVPMDTPGVTIIRPLSVFgyddAPHGHAEITFDNVRVPASNLILGEGRGFEIAQGRLGPGRIHH 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 267 AAAALGMARRALAEAVHHARQRRMFGQTLADFQLTQARIGEMAALVDSAALLTYRAAWLRDQ-GQARVTAEAAMAKMTAT 345
Cdd:cd01155 260 CMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAKSRIEIEQARLLVLKAAHMIDTvGNKAARKEIAMIKVAAP 339
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 496182615 346 ENAQRVIDMALQLHGGRGVEVGSKVESLYRDIRSLRIYEGATEVQQLIIGKAALQ 400
Cdd:cd01155 340 RMALKIIDRAIQVHGAAGVSQDTPLANMYAWARTLRIADGPDEVHLRSIARMELK 394
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
108-401 |
4.54e-39 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 143.82 E-value: 4.54e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 108 GSGAITLAGSPAQQAHYLQGVARGELIAAFALSEPEAGSDVSAMQTvatsaypsTASGKEHSYSLTGTKTWISNGGIADF 187
Cdd:PRK03354 93 GFNTFLREGTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLKT--------TYTRRNGKVYLNGSKCFITSSAYTPY 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 188 YCVFAKtDPAGGTRGI-SAFIVDANTPGLDASR-HIHVMAPHPLATLLFTNCTVPATALLGEENGGFKLAMRTLDIFRAS 265
Cdd:PRK03354 165 IVVMAR-DGASPDKPVyTEWFVDMSKPGIKVTKlEKLGLRMDSCCEITFDDVELDEKDMFGREGNGFNRVKEEFDHERFL 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 266 VAAAALGMARRALAEAVHHARQRRMFGQTLADFQLTQARIGEMAALVDSAALLTYRAAWLRDQGQArVTAEAAMAKMTAT 345
Cdd:PRK03354 244 VALTNYGTAMCAFEDAARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTI-TSGDAAMCKYFCA 322
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 496182615 346 ENAQRVIDMALQLHGGRGVEVGSKVESLYRDIRSLRIYEGATEVQQLIIGKAALQE 401
Cdd:PRK03354 323 NAAFEVVDSAMQVLGGVGIAGNHRISRFWRDLRVDRVSGGSDEMQILTLGRAVLKQ 378
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
55-390 |
1.29e-36 |
|
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). Mitochondrial acyl-CoA dehydrogenases (ACAD) catalyze the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. The mitochondrial ACD's are generally homotetramers and have an active site glutamate at a conserved position.
Pssm-ID: 173842 [Multi-domain] Cd Length: 407 Bit Score: 137.91 E-value: 1.29e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 55 VQRLGAGGWLRYCVPAAHGG-ALPaldsralvllretLAYHSPLADFAFA-------MQGLGSGAITLA--GSPAQQAHY 124
Cdd:cd01153 42 LDAFAEAGWMALGVPEEYGGqGLP-------------ITVYSALAEIFSRgdaplmyASGTQGAAATLLahGTEAQREKW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 125 LQGVARGELIAAFALSEPEAGSDVSAMQTVATSAypstasgKEHSYSLTGTKTWISNG--GIAD--FYCVFAKTDPAG-G 199
Cdd:cd01153 109 IPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQ-------ADGSWRINGVKRFISAGehDMSEniVHLVLARSEGAPpG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 200 TRGISAFIV-----DANTPGLDASRHIHVMAPHPLAT--LLFTNCTVPataLLGEENGGFKLAMRTLDIFRASVAAAALG 272
Cdd:cd01153 182 VKGLSLFLVpkfldDGERNGVTVARIEEKMGLHGSPTceLVFDNAKGE---LIGEEGMGLAQMFAMMNGARLGVGTQGTG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 273 MARRALAEAVHHARQRRMFGQTLADF-------QLTQAR-IGEMAALVDSAALLTYRAAWLRDQGQARVTAEAA------ 338
Cdd:cd01153 259 LAEAAYLNALAYAKERKQGGDLIKAApavtiihHPDVRRsLMTQKAYAEGSRALDLYTATVQDLAERKATEGEDrkalsa 338
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 496182615 339 -------MAKMTATENAQRVIDMALQLHGGRGVEVGSKVESLYRDIRSLRIYEGATEVQ 390
Cdd:cd01153 339 ladlltpVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEGTTGIQ 397
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
33-392 |
2.16e-33 |
|
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of several genes involved in the SOS adaptive response to DNA alkylation damage, whose expression is activated by the Ada protein. Its function has not been entirely elucidated; however, it is similar in sequence and function to acyl-CoA dehydrogenases. It has been proposed that aidB directly destroys DNA alkylating agents such as nitrosoguanidines (nitrosated amides) or their reaction intermediates.
Pssm-ID: 173843 [Multi-domain] Cd Length: 418 Bit Score: 129.03 E-value: 2.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 33 LVPWAA-AQEVDETDDRAACRDWVQRL-GAGGWLRYCVPAAHGGALPALDSRALVllretlayHSPLADFAFAMQGLGSG 110
Cdd:cd01154 48 LEMWDRwGRRVDRVWVHPAWHALMRRLiEEGVINIEDGPAGEGRRHVHFAAGYLL--------SDAAAGLLCPLTMTDAA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 111 AITL-AGSPAQQAHYLQGVA----RGELIAAFALSEPEAGSDVSAMQTVATSAYPSTasgkehsYSLTGTKtWISNGGIA 185
Cdd:cd01154 120 VYALrKYGPEELKQYLPGLLsdryKTGLLGGTWMTEKQGGSDLGANETTAERSGGGV-------YRLNGHK-WFASAPLA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 186 DFYCVFAKTDPA-GGTRGISAFIVDANTPglDASRHIHVMA---------PHPLATLLFTNctvpATA-LLGEENGGFKL 254
Cdd:cd01154 192 DAALVLARPEGApAGARGLSLFLVPRLLE--DGTRNGYRIRrlkdklgtrSVATGEVEFDD----AEAyLIGDEGKGIYY 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 255 AMRTLDIFRASVAAAALGMARRALAEAVHHARQRRMFGQTLADFQLTQARIGEMAALVDSAALLTYRAAWLRDQGQARVT 334
Cdd:cd01154 266 ILEMLNISRLDNAVAALGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAARAFDRAAADKP 345
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496182615 335 AEAAMA-------KMTATENAQRVIDMALQLHGGRGVEVGSKVESLYRDIRSLRIYEGATEVQQL 392
Cdd:cd01154 346 VEAHMArlatpvaKLIACKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQAL 410
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
98-396 |
6.85e-30 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 119.19 E-value: 6.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 98 ADFAFAMQGLGSGAITLAGSPAQQAHYLQGVARGELIAAFALSEPEAGSDVSAMQTVATSAypstasgkEHSYSLTGTKT 177
Cdd:PLN02526 107 STFILVHSSLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKV--------EGGWILNGQKR 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 178 WISNGGIADFYCVFAKTDpagGTRGISAFIVDANTPGLDASRHIHVMAPHPL--ATLLFTNCTVPATALLGEENgGFKLA 255
Cdd:PLN02526 179 WIGNSTFADVLVIFARNT---TTNQINGFIVKKGAPGLKATKIENKIGLRMVqnGDIVLKDVFVPDEDRLPGVN-SFQDT 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 256 MRTLDIFRASVAAAALGMARRALAEAVHHARQRRMFGQTLADFQLTQARIGEMAALVDSAALLTYRAAWLRDQGQArVTA 335
Cdd:PLN02526 255 NKVLAVSRVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMLGNIQAMFLVGWRLCKLYESGKM-TPG 333
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496182615 336 EAAMAKMTATENAQRVIDMALQLHGGRGVEVGSKVESLYRDIRSLRIYEGATEVQQLIIGK 396
Cdd:PLN02526 334 HASLGKAWITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDINALVTGR 394
|
|
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
116-400 |
4.04e-29 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 119.51 E-value: 4.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 116 GSPAQQAHYLQGVARGELIAAFALSEPE-AGSDVSAMQTvatsaypsTASGKEHSYSLTGTKTWISngGIADFYC----V 190
Cdd:PLN02876 533 GNKEQQLEWLIPLLEGKIRSGFAMTEPQvASSDATNIEC--------SIRRQGDSYVINGTKWWTS--GAMDPRCrvliV 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 191 FAKTDP-AGGTRGISAFIVDANTPGLDASRHIHVM----APHPLATLLFTNCTVPATALLGEENGGFKLAMRTLDIFRAS 265
Cdd:PLN02876 603 MGKTDFnAPKHKQQSMILVDIQTPGVQIKRPLLVFgfddAPHGHAEISFENVRVPAKNILLGEGRGFEIAQGRLGPGRLH 682
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 266 VAAAALGMARRALAEAVHHARQRRMFGQTLADFQLTQARIGEMAALVDSAALLTYRAAWLRDQ-GQARVTAEAAMAKMTA 344
Cdd:PLN02876 683 HCMRLIGAAERGMQLMVQRALSRKAFGKLIAQHGSFLSDLAKCRVELEQTRLLVLEAADQLDRlGNKKARGIIAMAKVAA 762
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 496182615 345 TENAQRVIDMALQLHGGRGVEVGSKVESLYRDIRSLRIYEGATEVQQLIIGKAALQ 400
Cdd:PLN02876 763 PNMALKVLDMAMQVHGAAGVSSDTVLAHLWATARTLRIADGPDEVHLGTIAKLELQ 818
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
136-225 |
1.77e-23 |
|
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a beta-barrel fold.
Pssm-ID: 460685 [Multi-domain] Cd Length: 95 Bit Score: 93.50 E-value: 1.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 136 AFALSEPEAGSDVSAMQTVAtsaypstASGKEHSYSLTGTKTWISNGGIADFYCVFAKTDPAGGTRGISAFIVDANTPGL 215
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTA-------ADGDGGGWVLNGTKWWITNAGIADLFLVLARTGGDDRHGGISLFLVPKDAPGV 73
|
90
....*....|
gi 496182615 216 DASRHIHVMA 225
Cdd:pfam02770 74 SVRRIETKLG 83
|
|
| Acyl-CoA_dh_2 |
pfam08028 |
Acyl-CoA dehydrogenase, C-terminal domain; |
265-388 |
1.58e-21 |
|
Acyl-CoA dehydrogenase, C-terminal domain;
Pssm-ID: 429790 [Multi-domain] Cd Length: 133 Bit Score: 89.33 E-value: 1.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 265 SVAAAALGMARRALAEAVHHARQRRM--FGQTLADFQLTQARIGEMAALVDSAALLTYRAAW----LRDQGQA---RVTA 335
Cdd:pfam08028 1 GIAAAALGAARAALAEFTERARGRVRayFGVPLAEDPATQLALAEAAARIDAARLLLERAAArieaAAAAGKPvtpALRA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 496182615 336 EAAMAKMTATENAQRVIDMALQLHGGRGVEVGSKVESLYRDIRSLRIYEGATE 388
Cdd:pfam08028 81 EARRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAVNP 133
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
56-399 |
1.67e-20 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 93.39 E-value: 1.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 56 QRLGAGGWLRYCVPAAHGG-ALPAldSRALVLlRETLAyhspLADFAFAM-QGLGSGA---ITLAGSPAQQAHYLQGVAR 130
Cdd:PTZ00456 106 QALKAGGWTGISEPEEYGGqALPL--SVGFIT-RELMA----TANWGFSMyPGLSIGAantLMAWGSEEQKEQYLTKLVS 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 131 GELIAAFALSEPEAGSDVSAMQTVATSAypstASGkehSYSLTGTKTWISNGGiADF-----YCVFAKT-DPAGGTRGIS 204
Cdd:PTZ00456 179 GEWSGTMCLTEPQCGTDLGQVKTKAEPS----ADG---SYKITGTKIFISAGD-HDLtenivHIVLARLpNSLPTTKGLS 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 205 AFIVDANTP----GLDASRHIHV------MAPHPLAT--LLFTNCTvpaTALLGEENGGFKLAMRTLDIFRASVAAAALG 272
Cdd:PTZ00456 251 LFLVPRHVVkpdgSLETAKNVKCiglekkMGIKGSSTcqLSFENSV---GYLIGEPNAGMKQMFTFMNTARVGTALEGVC 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 273 MARRALAEAVHHARQRR----------------------------MFGQTLADfqltqariGEMAALVDSAALLTYRA-- 322
Cdd:PTZ00456 328 HAELAFQNALRYARERRsmralsgtkepekpadriichanvrqniLFAKAVAE--------GGRALLLDVGRLLDIHAaa 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 323 --AWLRDQGQARVTAEAAMAKMTATENAQRVIDMALQLHGGRGVEVGSKVESLYRDIRSLRIYEGATEVQQL-IIGKAAL 399
Cdd:PTZ00456 400 kdAATREALDHEIGFYTPIAKGCLTEWGVEAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYEGTTGIQALdFIGRKVL 479
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
116-367 |
1.44e-18 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 87.95 E-value: 1.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 116 GSPAQQAHYLQGVARGELIAAFALSEPEAGSDVSAMqtvatsayPSTA-------SGKEHSY-SLTGTKTWISNGGIADf 187
Cdd:PRK09463 176 GTDEQKDHYLPRLARGEEIPCFALTSPEAGSDAGSI--------PDTGvvckgewQGEEVLGmRLTWNKRYITLAPIAT- 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 188 ycV----FAKTDP---AGGTR--GISAFIVDANTPGLD-ASRHIHVMAPhplatllFTNCT-------VPATALLGEENG 250
Cdd:PRK09463 247 --VlglaFKLYDPdglLGDKEdlGITCALIPTDTPGVEiGRRHFPLNVP-------FQNGPtrgkdvfIPLDYIIGGPKM 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 251 ---GFKLAMRTLDIFRA----SVAAAALGMARRALAEavhHARQRRMFGQTLADFQLTQ---ARIGEMAALVDSAALLTY 320
Cdd:PRK09463 318 agqGWRMLMECLSVGRGislpSNSTGGAKLAALATGA---YARIRRQFKLPIGKFEGIEeplARIAGNAYLMDAARTLTT 394
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 496182615 321 RAAwlrDQGQ--ARVTAeaaMAKMTATENAQRVIDMALQLHGGRGVEVG 367
Cdd:PRK09463 395 AAV---DLGEkpSVLSA---IAKYHLTERGRQVINDAMDIHGGKGICLG 437
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
116-369 |
1.20e-17 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 85.01 E-value: 1.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 116 GSPAQQAHYLQGVARGELIAAFALSEPEAGSDVSAMQTVATSAYpSTASGKEH-SYSLTGTKTWISNGGIADFY-CVFAK 193
Cdd:PRK13026 175 GTQEQKDYWLPRLADGTEIPCFALTGPEAGSDAGAIPDTGIVCR-GEFEGEEVlGLRLTWDKRYITLAPVATVLgLAFKL 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 194 TDPAG-----GTRGISAFIVDANTPGLD-ASRHIHVMAPhplatllFTNCT-------VPATALLG--EENG-GFKLAMR 257
Cdd:PRK13026 254 RDPDGllgdkKELGITCALIPTDHPGVEiGRRHNPLGMA-------FMNGTtrgkdvfIPLDWIIGgpDYAGrGWRMLVE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 258 TLDIFRA-SVAAAALGMARRALAEAVHHARQRRMFGQTLADFQLTQARIGEMAA---LVDSAALLTYRAAwlrDQGQ--A 331
Cdd:PRK13026 327 CLSAGRGiSLPALGTASGHMATRTTGAYAYVRRQFGMPIGQFEGVQEALARIAGntyLLEAARRLTTTGL---DLGVkpS 403
|
250 260 270
....*....|....*....|....*....|....*...
gi 496182615 332 RVTaeaAMAKMTATENAQRVIDMALQLHGGRGVEVGSK 369
Cdd:PRK13026 404 VVT---AIAKYHMTELARDVVNDAMDIHAGKGIQLGPK 438
|
|
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
82-385 |
2.82e-13 |
|
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in the peroxisomal fatty acid beta-oxidation, the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. In a second oxidative half-reaction, the reduced FAD is reoxidized by molecular oxygen. AXO is generally a homodimer, but it has been reported to form a different type of oligomer in yeast. There are several subtypes of AXO's, based on substrate specificity. Palmitoyl-CoA oxidase acts on straight-chain fatty acids and prostanoids; whereas, the closely related Trihydroxycoprostanoly-CoA oxidase has the greatest activity for 2-methyl branched side chains of bile precursors. Pristanoyl-CoA oxidase, acts on 2-methyl branched fatty acids. AXO has an additional domain, C-terminal to the region with similarity to acyl-CoA dehydrogenases, which is included in this alignment.
Pssm-ID: 173839 [Multi-domain] Cd Length: 610 Bit Score: 71.21 E-value: 2.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 82 RALVLLRETLAYHSPLADFAFAMQGLGSGAITLAGSPAQQAHYLQGVARGELIAAFALSEPEAGSDVSAMQTVATsaY-P 160
Cdd:cd01150 83 KMLALTNSLGGYDLSLGAKLGLHLGLFGNAIKNLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTAT--YdP 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 161 STASGKEHSYSLTGTKTWISNGGI-ADFYCVFAKTDPAGGTRGISAFIV---DANT----PGLDasrhIHVMAPHPL--- 229
Cdd:cd01150 161 LTQEFVINTPDFTATKWWPGNLGKtATHAVVFAQLITPGKNHGLHAFIVpirDPKThqplPGVT----VGDIGPKMGlng 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 230 ---ATLLFTNCTVPATALLG----------------EENGGFKLAMRTLDIFRASVAAAALGMARRALAEAVHHARQRRM 290
Cdd:cd01150 237 vdnGFLQFRNVRIPRENLLNrfgdvspdgtyvspfkDPNKRYGAMLGTRSGGRVGLIYDAAMSLKKAATIAIRYSAVRRQ 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 291 FGQT-------LADFQLTQARIGEMAAlvdSAALLTYRAAWLRD----------QGQARVTAE----AAMAKMTATENAQ 349
Cdd:cd01150 317 FGPKpsdpevqILDYQLQQYRLFPQLA---AAYAFHFAAKSLVEmyheiikellQGNSELLAElhalSAGLKAVATWTAA 393
|
330 340 350
....*....|....*....|....*....|....*.
gi 496182615 350 RVIDMALQLHGGRGVEVGSKVESLYRDIRSLRIYEG 385
Cdd:cd01150 394 QGIQECREACGGHGYLAMNRLPTLRDDNDPFCTYEG 429
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
23-132 |
1.42e-11 |
|
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is an all-alpha domain.
Pssm-ID: 460686 [Multi-domain] Cd Length: 113 Bit Score: 60.94 E-value: 1.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 23 DDAHRTLAEGLVPWAAaqEVDETDDRAacRDWVQRLGAGGWLRYCVPAAHGGAlpALDSRALVLLRETLAY-HSPLADFA 101
Cdd:pfam02771 9 DTVREFAEEEIAPHAA--EWDEEGEFP--RELWKKLGELGLLGITIPEEYGGA--GLDYLAYALVAEELARaDASVALAL 82
|
90 100 110
....*....|....*....|....*....|.
gi 496182615 102 FAMQGLGSGAITLAGSPAQQAHYLQGVARGE 132
Cdd:pfam02771 83 SVHSSLGAPPILRFGTEEQKERYLPKLASGE 113
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
27-338 |
3.51e-10 |
|
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, which catalyzes the first two steps of DBT desulfurization in mesophilic bacteria. DszC converts DBT to DBT-sulfoxide, which is then converted to DBT-sulfone. Bacteria with this enzyme are candidates for the removal of organic sulfur compounds from fossil fuels, which pollute the environment. An equivalent enzyme tdsC, is found in thermophilic bacteria. This alignment also contains a closely related uncharacterized subgroup.
Pssm-ID: 173852 [Multi-domain] Cd Length: 377 Bit Score: 61.18 E-value: 3.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 27 RTLAEGLVPWAAAQEvdetDDRAACRDWVQRLGAGGWLRYCVPAAHGGALPALDSrALVLLRETLAYHSPLADfAFAMQG 106
Cdd:cd01163 4 RPLAARIAEGAAERD----RQRGLPYEEVALLRQSGLGTLRVPKEYGGLGASLPD-LYEVVRELAAADSNIAQ-ALRAHF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 107 LGSGAITLAGSPAQQAHYLQGVARGELIAAfALSEpeagSDVSAMQTVATSaypsTASGKEHsYSLTGTKTWISNGGIAD 186
Cdd:cd01163 78 GFVEALLLAGPEQFRKRWFGRVLNGWIFGN-AVSE----RGSVRPGTFLTA----TVRDGGG-YVLNGKKFYSTGALFSD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 187 FYCVFAkTDPAGGtrgISAFIVDANTPGLDASRHIHVMAPHPLA--TLLFTNCTVPATALLGEENGGFKLAMRTLdIFRA 264
Cdd:cd01163 148 WVTVSA-LDEEGK---LVFAAVPTDRPGITVVDDWDGFGQRLTAsgTVTFDNVRVEPDEVLPRPNAPDRGTLLTA-IYQL 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496182615 265 SVAAAALGMARRALAEAVHHARQR-RMFG----QTLADFQLTQARIGEMAALVDSAALLTYRAAWLRDQGQARVTAEAA 338
Cdd:cd01163 223 VLAAVLAGIARAALDDAVAYVRSRtRPWIhsgaESARDDPYVQQVVGDLAARLHAAEALVLQAARALDAAAAAGTALTA 301
|
|
| PRK11561 |
PRK11561 |
isovaleryl CoA dehydrogenase; Provisional |
122-392 |
1.65e-08 |
|
isovaleryl CoA dehydrogenase; Provisional
Pssm-ID: 183199 [Multi-domain] Cd Length: 538 Bit Score: 56.30 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 122 AHYLQGVARGELIAAFALSEPEAGSDVSAMQTVATSAypstasgKEHSYSLTGTKtWISNGGIADFYCVFAKTDpaggtR 201
Cdd:PRK11561 167 SHLLPGGQKRGLLIGMGMTEKQGGSDVLSNTTRAERL-------ADGSYRLVGHK-WFFSVPQSDAHLVLAQAK-----G 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 202 GISAFIVDANTPglDASRHIHVMA--PHPLATLLFTNCTVP---ATA-LLGEENGGFKLAMRTLDIFRASVAAAALGMAR 275
Cdd:PRK11561 234 GLSCFFVPRFLP--DGQRNAIRLErlKDKLGNRSNASSEVEfqdAIGwLLGEEGEGIRLILKMGGMTRFDCALGSHGLMR 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 276 RALAEAVHHARQRRMFGQTLADFQLTQARIGEMAALVD--SAALLTYRAAWLRdQGQARVTAEAAM----AKMTATENAQ 349
Cdd:PRK11561 312 RAFSVAIYHAHQRQVFGKPLIEQPLMRQVLSRMALQLEgqTALLFRLARAWDR-RADAKEALWARLftpaAKFVICKRGI 390
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 496182615 350 RVIDMALQLHGGRGVEVGSKVESLYRDIRSLRIYEGATEVQQL 392
Cdd:PRK11561 391 PFVAEAMEVLGGIGYCEESELPRLYREMPVNSIWEGSGNIMCL 433
|
|
| NcnH |
cd01159 |
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ... |
262-381 |
1.03e-07 |
|
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, which is active against Gram-positive bacteria. Polyketides are secondary metabolites, which have important biological functions such as antitumor, immunosupressive or antibiotic activities. NcnH is a hydroxylase involved in the biosynthesis of naphthocyclinone and possibly other polyketides.
Pssm-ID: 173848 [Multi-domain] Cd Length: 370 Bit Score: 53.51 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 262 FRASVAAAALGMARRALAEAVHHARQRRM---FGQTLADFQLTQARIGEMAALVDSAALLTYRAAWLRDQGQARVTAEAA 338
Cdd:cd01159 221 FPLSFAAVSLGAAEGALAEFLELAGKRVRqygAAVKMAEAPITQLRLAEAAAELDAARAFLERATRDLWAHALAGGPIDV 300
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 496182615 339 MAKMT-------ATENAQRVIDMALQLHGGRGVEVGSKVESLYRDIRSLR 381
Cdd:cd01159 301 EERARirrdaayAAKLSAEAVDRLFHAAGGSALYTASPLQRIWRDIHAAA 350
|
|
| PTZ00460 |
PTZ00460 |
acyl-CoA dehydrogenase; Provisional |
132-305 |
1.15e-05 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185639 [Multi-domain] Cd Length: 646 Bit Score: 47.53 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 132 ELIAAFALSEPEAGSDVSAMQTVATSAyPSTASGKEHSYSLTGTKTWISN-GGIADFYCVFAKTDPAGGTRGISAFIV-- 208
Cdd:PTZ00460 126 EIVGCYAQTELGHGSDVQNLETTATYD-KQTNEFVIHTPSVEAVKFWPGElGFLCNFALVYAKLIVNGKNKGVHPFMVri 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 209 -DANT----PGLDasrhIHVMAPHPLAT------LLFTNCTVPATALLGE-----ENGGF------KLAMRTLDIFRASV 266
Cdd:PTZ00460 205 rDKEThkplQGVE----VGDIGPKMGYAvkdngfLSFDHYRIPLDSLLARyikvsEDGQVerqgnpKVSYASMMYMRNLI 280
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 496182615 267 AAAALGMARRALAEAVHHARQRRMF----GQ--TLADFQLTQARI 305
Cdd:PTZ00460 281 IDQYPRFAAQALTVAIRYSIYRQQFtndnKQenSVLEYQTQQQKL 325
|
|
| PLN02636 |
PLN02636 |
acyl-coenzyme A oxidase |
107-310 |
4.80e-04 |
|
acyl-coenzyme A oxidase
Pssm-ID: 215342 [Multi-domain] Cd Length: 686 Bit Score: 42.15 E-value: 4.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 107 LGSGAITLAGSPAQQAHYLQGVARGELIAAFALSEPEAGSDVSAMQTVATSAyPSTASGKEHSYSLTGTKTWISNGGI-A 185
Cdd:PLN02636 147 LWGGSVINLGTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTATFD-PLTDEFVINTPNDGAIKWWIGNAAVhG 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 186 DFYCVFAKT-----DPAGGT-RGISAFIV---DANT----PGLDASRHIHVMAPHPL--ATLLFTNCTVPATALLGE--- 247
Cdd:PLN02636 226 KFATVFARLklpthDSKGVSdMGVHAFIVpirDMKThqvlPGVEIRDCGHKVGLNGVdnGALRFRSVRIPRDNLLNRfgd 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 248 --ENGGFKLAMRTLDIF-----------RASVAAAALGMARRALAEAVHHARQRRMFGQ------TLADFQLTQARIGEM 308
Cdd:PLN02636 306 vsRDGKYTSSLPTINKRfaatlgelvggRVGLAYGSVGVLKASNTIAIRYSLLRQQFGPpkqpeiSILDYQSQQHKLMPM 385
|
..
gi 496182615 309 AA 310
Cdd:PLN02636 386 LA 387
|
|
| PLN02443 |
PLN02443 |
acyl-coenzyme A oxidase |
111-208 |
6.16e-04 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178062 [Multi-domain] Cd Length: 664 Bit Score: 42.13 E-value: 6.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182615 111 AITLAGSPAQQAHYLQGVARGELIAAFALSEPEAGSDVSAMQTVATSAyPSTASGKEHSYSLTGTKTWISNGGIADFYC- 189
Cdd:PLN02443 109 AIKGQGTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTATFD-PKTDEFVIHSPTLTSSKWWPGGLGKVSTHAv 187
|
90
....*....|....*....
gi 496182615 190 VFAKTDPAGGTRGISAFIV 208
Cdd:PLN02443 188 VYARLITNGKDHGIHGFIV 206
|
|
| |
